4O22: Binary complex of metal-free PKAc with SP20

Binary complex of metal-free PKAc with SP20. Determined by X-ray diffraction at 1.7 Å resolution. Released 28 May 2014.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 3,256
Mol. weight: 42.43 kDa
Released: 28 May 2014

Explore 4O22 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4O22 contains 21 α-helices and 15 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	13-31	19
α-helix	40-42	3
β-strand	43-51	9	1
β-strand	55-62	8	1
β-strand	68-75	8	1
α-helix	76-81	6
α-helix	85-95	11
β-strand	103	1	2
α-helix	104-105	2
β-strand	106-111	6	1
β-strand	115-121	7	1
α-helix	122	1
β-strand	127	1	2
α-helix	128-135	8
α-helix	140-159	20
β-strand	162-163	2	3
α-helix	169-171	3
β-strand	172-174	3	2
β-strand	180-182	3	2
β-strand	189-190	2	3
β-strand	195	1	4
β-strand	199-200	2	5
α-helix	202-204	3
α-helix	207-210	4
β-strand	215	1	4
α-helix	218-233	16
α-helix	243-252	10
α-helix	263-272	10
α-helix	277-279	3
α-helix	289-292	4
α-helix	295-297	3
α-helix	302-306	5
α-helix	311-312	2

Chain S: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	606-611	6
α-helix	618-621	4
β-strand	622-623	2	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cAMP-dependent protein kinase catalytic subunit alpha.	A	protein	342	Mus musculus	P05132 (AlphaFold model)
Phosphorylated peptide pSP20.	S	protein	20	Homo sapiens	P61925 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4O22_1 cAMP-dependent protein kinase catalytic subunit alpha. (chains A)
HHHHHHVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNH
YAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEM
FSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFA
KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYE
KIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQR
KVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF

Sequence of entity 2 (S), FASTA

>4O22_2 Phosphorylated peptide pSP20. (chains S)
TTYADFIASGRTGRRASIHD

Primary citation

Metal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl Transfer. Gerlits, O., Das, A., Keshwani, M.M. et al. Biochemistry (2014) 53:3179-3186. DOI 10.1021/bi5000965 · PubMed

Other PDB entries of the same protein (UniProt P05132 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1RDQ 1.26 Å, Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase
4DFX 1.35 Å, Crystal structure of myristoylated K7C catalytic subunit of cAMP-dependent protein…
4HPU 1.55 Å, Crystal structure of the catalytic subunit of cAMP-dependent protein kinase displaying…
4IAI 1.55 Å, X-ray Structure of cAMP dependent protein kinase A in complex with high Ca2+…
9PC1 1.55 Å, Co-crystal structure of the cAMP-dependent protein kinase catalytic subunit alpha with…
3FJQ 1.6 Å, Crystal structure of cAMP-dependent protein kinase catalytic subunit alpha in complex…
4IAK 1.6 Å, Low temperature X-ray structure of cAMP dependent protein kinase A in complex with high…
3IDB 1.62 Å, Crystal structure of (108-268)RIIb:C holoenzyme of cAMP-dependent protein kinase
4IB1 1.63 Å, Structure of cAMP dependent protein kinase A in complex with high K+ concentration, ADP…
7V0G 1.63 Å, Structure of cAMP-dependent protein kinase using a MD-MX procedure, produced using 1.63…
3QAL 1.7 Å, Crystal Structure of Arg280Ala mutant of Catalytic subunit of cAMP-dependent Protein…
3X2W 1.7 Å, Michaelis complex of cAMP-dependent Protein Kinase Catalytic Subunit

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